Phycobilisome protein ApcG interacts with PSII and regulates energy transfer in Synechocystis
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články
Grantová podpora
Howard Hughes Medical Institute - United States
PubMed
37972281
PubMed Central
PMC10904348
DOI
10.1093/plphys/kiad615
PII: 7424862
Knihovny.cz E-zdroje
- MeSH
- fotosystém I (proteinový komplex) metabolismus MeSH
- fotosystém II (proteinový komplex) metabolismus MeSH
- fykobilizomy metabolismus MeSH
- přenos energie fyziologie MeSH
- Synechocystis * metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- fotosystém I (proteinový komplex) MeSH
- fotosystém II (proteinový komplex) MeSH
- fykobilizomy MeSH
Photosynthetic organisms harvest light using pigment-protein complexes. In cyanobacteria, these are water-soluble antennae known as phycobilisomes (PBSs). The light absorbed by PBS is transferred to the photosystems in the thylakoid membrane to drive photosynthesis. The energy transfer between these complexes implies that protein-protein interactions allow the association of PBS with the photosystems. However, the specific proteins involved in the interaction of PBS with the photosystems are not fully characterized. Here, we show in Synechocystis sp. PCC 6803 that the recently discovered PBS linker protein ApcG (sll1873) interacts specifically with PSII through its N-terminal region. Growth of cyanobacteria is impaired in apcG deletion strains under light-limiting conditions. Furthermore, complementation of these strains using a phospho-mimicking version of ApcG causes reduced growth under normal growth conditions. Interestingly, the interaction of ApcG with PSII is affected when a phospho-mimicking version of ApcG is used, targeting the positively charged residues interacting with the thylakoid membrane, suggesting a regulatory role mediated by phosphorylation of ApcG. Low-temperature fluorescence measurements showed decreased PSI fluorescence in apcG deletion and complementation strains. The PSI fluorescence was the lowest in the phospho-mimicking complementation strain, while the pull-down experiment showed no interaction of ApcG with PSI under any tested condition. Our results highlight the importance of ApcG for selectively directing energy harvested by the PBS and imply that the phosphorylation status of ApcG plays a role in regulating energy transfer from PSII to PSI.
Department of Biochemistry and Molecular Biology Michigan State University East Lansing MI 48824 USA
Department of Plant and Microbial Biology University of California Berkeley CA 94720 USA
Howard Hughes Medical Institute University of California Berkeley CA 94720 USA
MSU DOE Plant Research Laboratory Michigan State University East Lansing MI 48824 USA
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